| IED ID | IndEnz0001000818 |
| Enzyme Type ID | amylase000818 |
| Protein Name |
1,4-alpha-glucan-branching enzyme EC 2.4.1.18 Brancher enzyme Glycogen-branching enzyme |
| Gene Name | Gbe1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAAPAAPAAGETGPDARLEAALADVPELARLLEIDPYLKPFAADFQRRYKKFSQVLHDIGENEGGIDKFSRGYESFGIHRCSDGGIYCKEWAPGAEGVFLTGEFSGWNPFSHPYKKLEYGKWELYIPPKQNKSPLIPHGSKLKVVITSKSGEILYRISPWAKYVVRENNNVNYDWIHWAPEDPYKFKHSRPKKPRSLRIYESHVGISSHEGKIASYKHFTSNVLPRIKDLGYNCIQLMAIMEHAYYASFGYQITSFFAASSRYGTPEELKELVDTAHSMGIVVLLDVVHSHASKNSEDGLNMFDGTDSCYFHSGPRGTHDLWDSRLFIYSSWEVLRFLLSNIRWWLEEYCFDGFRFDGVTSMLYHHHGMGQGFSGDYNEYFGLQVDEDALIYLMLANHLAHTLYPDSITIAEDVSGMPALCSPTSQGGGGFDYRLAMAIPDKWIQLLKEFKDEDWNMGNIVYTLTNRRYLEKCVAYAESHDQALVGDKTLAFWLMDAEMYTNMSVLAPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEWLDFPRKGNNESYHYARRQFNLTDDDLLRYKFLNNFDRDMNRLEERCGWLSAPQAYVSEKHEANKTITFERAGLLFIFNFHPSKSYTDYRVGTATPGKFKIVLDSDAAEYGGHQRLDHNTNYFAEAFEHNGRPYSLLVYIPSRVALILQNVDLQN |
| Enzyme Length | 702 |
| Uniprot Accession Number | Q9D6Y9 |
| Absorption | |
| Active Site | ACT_SITE 357; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 412; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; Evidence={ECO:0000250|UniProtKB:Q04446}; |
| DNA Binding | |
| EC Number | 2.4.1.18 |
| Enzyme Function | FUNCTION: Required for normal glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule. {ECO:0000250|UniProtKB:Q04446}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000250|UniProtKB:Q04446}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Initiator methionine (1); Modified residue (2); Region (4) |
| Keywords | Acetylation;Glycogen biosynthesis;Glycogen storage disease;Glycosyltransferase;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q04446; MOD_RES 173; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q04446 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11217851; 12466851; 14681479; 16075367; 16602821; 16615898; 17937387; 19884348; 20300197; 21075835; 21267068; 21677750; 21856731; 21862448; 26385640; 27215380; 27542691; 30185673; 31042462; 31917811; 32798765; 33049291; 33857563; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,364 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |